1jqk
From Proteopedia
(New page: 200px<br /><applet load="1jqk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jqk, resolution 2.8Å" /> '''Crystal structure of ...) |
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| - | [[Image:1jqk.gif|left|200px]]<br /><applet load="1jqk" size=" | + | [[Image:1jqk.gif|left|200px]]<br /><applet load="1jqk" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1jqk, resolution 2.8Å" /> | caption="1jqk, resolution 2.8Å" /> | ||
'''Crystal structure of carbon monoxide dehydrogenase from Rhodospirillum rubrum'''<br /> | '''Crystal structure of carbon monoxide dehydrogenase from Rhodospirillum rubrum'''<br /> | ||
==Overview== | ==Overview== | ||
| - | A crystal structure of the anaerobic Ni-Fe-S carbon monoxide dehydrogenase | + | A crystal structure of the anaerobic Ni-Fe-S carbon monoxide dehydrogenase (CODH) from Rhodospirillum rubrum has been determined to 2.8-A resolution. The CODH family, for which the R. rubrum enzyme is the prototype, catalyzes the biological oxidation of CO at an unusual Ni-Fe-S cluster called the C-cluster. The Ni-Fe-S C-cluster contains a mononuclear site and a four-metal cubane. Surprisingly, anomalous dispersion data suggest that the mononuclear site contains Fe and not Ni, and the four-metal cubane has the form [NiFe(3)S(4)] and not [Fe(4)S(4)]. The mononuclear site and the four-metal cluster are bridged by means of Cys(531) and one of the sulfides of the cube. CODH is organized as a dimer with a previously unidentified [Fe(4)S(4)] cluster bridging the two subunits. Each monomer is comprised of three domains: a helical domain at the N terminus, an alpha/beta (Rossmann-like) domain in the middle, and an alpha/beta (Rossmann-like) domain at the C terminus. The helical domain contributes ligands to the bridging [Fe(4)S(4)] cluster and another [Fe(4)S(4)] cluster, the B-cluster, which is involved in electron transfer. The two Rossmann domains contribute ligands to the active site C-cluster. This x-ray structure provides insight into the mechanism of biological CO oxidation and has broader significance for the roles of Ni and Fe in biological systems. |
==About this Structure== | ==About this Structure== | ||
| - | 1JQK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodospirillum_rubrum Rhodospirillum rubrum] with FE2, SF4, WCC and UNX as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Carbon-monoxide_dehydrogenase_(acceptor) Carbon-monoxide dehydrogenase (acceptor)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.99.2 1.2.99.2] Full crystallographic information is available from [http:// | + | 1JQK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodospirillum_rubrum Rhodospirillum rubrum] with <scene name='pdbligand=FE2:'>FE2</scene>, <scene name='pdbligand=SF4:'>SF4</scene>, <scene name='pdbligand=WCC:'>WCC</scene> and <scene name='pdbligand=UNX:'>UNX</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Carbon-monoxide_dehydrogenase_(acceptor) Carbon-monoxide dehydrogenase (acceptor)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.99.2 1.2.99.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JQK OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Rhodospirillum rubrum]] | [[Category: Rhodospirillum rubrum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Drennan, C | + | [[Category: Drennan, C L.]] |
[[Category: Heo, J.]] | [[Category: Heo, J.]] | ||
| - | [[Category: Ludden, P | + | [[Category: Ludden, P W.]] |
[[Category: Schreiter, E.]] | [[Category: Schreiter, E.]] | ||
| - | [[Category: Sintchak, M | + | [[Category: Sintchak, M D.]] |
[[Category: FE2]] | [[Category: FE2]] | ||
[[Category: SF4]] | [[Category: SF4]] | ||
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[[Category: rossmann fold]] | [[Category: rossmann fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:25:35 2008'' |
Revision as of 11:25, 21 February 2008
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Crystal structure of carbon monoxide dehydrogenase from Rhodospirillum rubrum
Overview
A crystal structure of the anaerobic Ni-Fe-S carbon monoxide dehydrogenase (CODH) from Rhodospirillum rubrum has been determined to 2.8-A resolution. The CODH family, for which the R. rubrum enzyme is the prototype, catalyzes the biological oxidation of CO at an unusual Ni-Fe-S cluster called the C-cluster. The Ni-Fe-S C-cluster contains a mononuclear site and a four-metal cubane. Surprisingly, anomalous dispersion data suggest that the mononuclear site contains Fe and not Ni, and the four-metal cubane has the form [NiFe(3)S(4)] and not [Fe(4)S(4)]. The mononuclear site and the four-metal cluster are bridged by means of Cys(531) and one of the sulfides of the cube. CODH is organized as a dimer with a previously unidentified [Fe(4)S(4)] cluster bridging the two subunits. Each monomer is comprised of three domains: a helical domain at the N terminus, an alpha/beta (Rossmann-like) domain in the middle, and an alpha/beta (Rossmann-like) domain at the C terminus. The helical domain contributes ligands to the bridging [Fe(4)S(4)] cluster and another [Fe(4)S(4)] cluster, the B-cluster, which is involved in electron transfer. The two Rossmann domains contribute ligands to the active site C-cluster. This x-ray structure provides insight into the mechanism of biological CO oxidation and has broader significance for the roles of Ni and Fe in biological systems.
About this Structure
1JQK is a Single protein structure of sequence from Rhodospirillum rubrum with , , and as ligands. Active as Carbon-monoxide dehydrogenase (acceptor), with EC number 1.2.99.2 Full crystallographic information is available from OCA.
Reference
Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase., Drennan CL, Heo J, Sintchak MD, Schreiter E, Ludden PW, Proc Natl Acad Sci U S A. 2001 Oct 9;98(21):11973-8. Epub 2001 Oct 2. PMID:11593006
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